› 5x5q

X-ray diffraction
2.79Å resolution

Human thymidylate synthase complexed with dUMP and raltitrexed

Released:
DOI: 10.2210/pdb5x5q/pdb
PDB entry 5x5q coloured by chain, front view.
PDB entry 5x5q coloured by chain, side view.
PDB entry 5x5q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analyses of human thymidylate synthase reveal a site that may control conformational switching between active and inactive states.
Chen D, Jansson A, Sim D, Larsson A, Nordlund P
J Biol Chem 292 13449-13458 (2017)
PMID: 28634233

Function and Biology Details

Reaction catalysed: 
5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138196 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thymidylate synthase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 290 amino acids
Theoretical weight: 33.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04818 (Residues: 26-313; Coverage: 92%)
Gene names: OK/SW-cl.29, TS, TYMS
Sequence domains: Thymidylate synthase
Structure domains: Thymidylate synthase/dCMP hydroxymethylase domain

Ligands and Environments

2 bound ligands:
Ligand UMP 6 x UMP
Ligand D16 6 x D16
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P43212
Unit cell:
a: 107.835Å b: 107.835Å c: 314.951Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.221 0.262
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Therapeutic targeting of the mitochondrial one-carbon pathway: perspectives, pitfalls, and potential.
Zhao et al. (2021)
2 more

8 mentions without citation

A Structure-Based Drug Discovery Paradigm.
Batool et al. (2019)
7 more